This study investigated the role of dietary prebiotic mannan-oligosaccharides (MOS), and probiotic Bifidobacterium bifidum (BFD) in lipid metabolism, deposition, and consequent health indices in broiler chicken. The supplementation of 0.2% MOS along with either 106 or 107 CFU BFD/g feed resulted in downregulation of Acetyl-CoA carboxylase, fatty acid synthase, sterolregulatory element binding protein-1, and apolipoprotein B100; and up-regulation of peroxisome proliferator activated receptor-α AMP-activated protein kinase α-1, and stearoyl CoA (∆9) desaturase-1 hepatic expression in broiler chicken. The birds supplemented with 0.2% MOS along with either 106 or 107 CFU BFD/g feed depicted lower body fat percentage, palmitic acid, stearic acid, and saturated fatty acid contents, whereas, higher palmitoleic acid, oleic acid, and MUFA contents were observed. The ∆9-desaturase indices of chicken meat have shown higher values; and elongase index (only thigh) and thioesterase index have shown lower values in birds supplemented with 0.2% MOS along with either 106 or 107 CFU BFD/g feed. The meat health indices such as Polyunsaturated fatty acids (PUFA)/Saturated fatty acids (SFA) ratio, Mono-saturated fatty acids (MUFA)/SFA ratio, unsaturated fatty acids (UFA)/SFA ratio, hypocholesterolemic/hypercholesterolemic fatty acid ratio, saturation index, atherogenic index, thrombogenic index, and hypercholesterolemic fatty acid content were positively improved in birds supplemented with 0.2% MOS along with either 106 or 107 CFU BFD/g feed. Similarly, the birds supplemented with 0.2% MOS along with either 106 or 107 CFU BFD/g feed have shown lower serum triglyceride and total cholesterol levels along with higher high density levels and improved serum health indices cardiac risk ratio, atherogenic coefficient, and, atherogenic index of plasma.

Background: Peptidyl-prolyl cis-trans isomerisation (PPIases) enzyme plays a vital role in protein folding. It catalyses the cis-trans isomerisation of peptide bonds, an essential step for newly synthesized protein to acquire its correct functional conformation in both prokaryotes and eukaryotes. Objective: The present study showed the biochemical and molecular characterisation of cyclophilins (PpiB), a type of peptidyl-prolyl isomerases proteins from the pathogenic bacteria Salmonella Typhimurium. Methods: Salmonella Typhimurium is one of the leading serovars responsible for human and animal salmonellosis globally, with the majority of human cases originating through the food chain. Here successful expression and purification of PpiB protein have been demonstrated and LC-MS based analyses showed high protein score and similarity with other PPi protein. Further the enzymatic activity of the purified recombinant PpiB was determined using Succinyl-Ala-Phe-Pro-Phe-p nitroanilide as substrate and enzyme-catalysed reaction. Result: Km and Vmax were calculated and found to be Vm = 1.023 ± .06400 min/µg, Km = 0.6219 ± 0.1701 µM, respectively.We have reported for the first time the presence of Salmonella PPIase-B (PpiB) protein isoforms in salmonella genome having PPi activity. Conclusion: Taken together, our data clearly showed that Salmonella Cyclophilin B (PpiB) protein is active and involved in diverse biological processes and highly similar to the different domain of Cyclophilin proteins.

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Salmonella Typhimurium (ST) is the zoonotic pathogenic Gram-negative bacteria to causes infectious disease in humans as well as in animals. It causes gastrointestinal illness and fever called salmonellosis, which is foodborne diarrheal and leading cause of millions of deaths worldwide. Salmonella enterica serovar Typhimurium (S. Typhimurium) during its pathogenesis takeaway the actin cytoskeleton of their host cells and this is the crucial step of its infection cycle. Cyclophilin A, a type of peptidyl-prolyl isomerase that’s encoded by the ppiA gene in ST, plays pleiotropic roles in maintaining bacterial physiology. In this research, the proteomic characterization of the peptidyl-prolyl cis-trans isomerase- A (Cyclophilin A) from Salmonella Typhimurium is reported. Cyclophilin A (CypA) protein from Salmonella Typhimurium proved to be a highly conserved protein sequence and highly homologous compared to other organisms. This protein was expressed in Escherichia coli and then purified in a recombinant form protein exhibited a characteristic PPIases activity (Vmax = 0.8752 ± 0.13892 µmoles/ min, Km = 0.9315 ± 0.5670 µM) in comparison to control. Also, in this study the mass spectrometry analysis of Cyp A protein-peptide showed the highest sequence similarity with the cyclophilin protein of Salmonella. PPIases proteins enzyme data suggest that Ppi-A has roles in the protein folding that may be contributing to the virulence of Salmonella by isomerization of protein outline. These results suggest an active and vital role of this protein in protein folding along with regulation in Salmonella Typhimurium.

Background Salmonella Typhimurium is a zoonotic pathogen responsible for food and waterborne gastroenteritis in humans. Salmonella Typhimurium expresses Universal stress proteins (USPs) when subjected to different biotic and abiotic stresses. This class of proteins is becoming widely recognizedfor its role in bacterial stress resistance and protracted growth arrest. USPs possesses versatile structures arising from the fusion of the USP domain with various other catalytic motifs; they are possibly involved in a variety of reactions and cellular activities under stressful conditions. Objective The aim of this study is to obtain the universal stress protein A (uspA) gene of Salmonella Typhimurium and clone it into the pET28C plasmid for nucleotide sequencing. And also 3D structure prediction of USPA protein and to evaluate its phylogenetic gene tree model. Methods In this study, we constructed a recombinant clone of the uspA (pET28c_uspA) gene from Salmonella Typhimurium, and various methods, including sequencing, did conformation to the clone. The sequence was subsequently submitted to the NCBI GenBank database. Besides, the Three-dimensional structure for USPA protein was predicted by comparative modeling. A phylogenetic gene tree was also constructed to trace the evolutionary history of the uspA gene of Salmonella Typhimurium. Results The uspA gene of 435 bp in length was successfully cloned. Comparing the uspA gene sequence with that reported in GenBank showed that identities were 100%. Furthermore, Sequence analysis also revealed the uspA gene is 435 bp long, encodes a protein of 144 amino acids with a calculated molecular mass of 16 kDa, and belongs to the USP family. Predicted 3D structure and sequence alignments of USPA showed that all residues’ sites are highly similar among the genome. The stereo-chemical property of the 3D structure of USPA was found to be of good quality. Conclusion A confirmed uspA gene from Salmonella Typhimurium was reported in this study. This study laid a solid foundation for recombination and research of genes. Moreover, the results of this study would help to detect the functional domains of the protein to elucidate their structural/functional characteristics.